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Integrative and Comparative Biology Advance Access originally published online on August 30, 2006
Integrative and Comparative Biology 2006 46(6):815-826; doi:10.1093/icb/icl035
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© The Author 2006. Published by Oxford University Press on behalf of the Society for Integrative and Comparative Biology. All rights reserved. For permissions please email: journals.permissions@oxfordjournals.org.

Evolution of the thyroid hormone, retinoic acid, ecdysone and liver X receptors

Noah Ollikainen*, Charlie Chandsawangbhuwana{dagger} and Michael E. Baker1,§
* Department of Biology, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0693, USA
{dagger} Department of Bioengineering, University of California, San Diego 9500 Gilman Drive, La Jolla, CA 92093-0693, USA
§ Department of Medicine, University of California, San Diego 9500 Gilman Drive, La Jolla, CA 92093-0693, USA

Correspondence: 1E-mail: mbaker{at}ucsd.edu

Ecdysone and thyroid hormone are 2 ligands that have important roles in regulating metamorphosis in animals. Ecdysone is a steroid that regulates molting in insects. Thyroid hormone regulates differentiation and development in fish and amphibia. Although ecdysone and thyroid hormone have different chemical structures, both hormones act by binding to transcription factors that belong to the nuclear receptor family. We investigated the evolution of structure and function in the ecdysone receptor (EcR) and thyroid hormone receptor (TR), and liver X receptor (LXR) and retinoic acid receptor (RAR), which cluster with EcR and TR, respectively (Bertrand S, Brunet FG, Escriva H, Parmentier G, Laudet V, Robinson-Rechavi M. 2004. Mol Biol Evol 21:1923–37), by constructing a multiple alignment of their sequences and calculating ancestral sequences for TR, RAR, EcR, and LXR. These alignments were mapped onto the 3D structures of TR, RAR, EcR, and LXR in the Protein Data Bank to examine the evolution of amino acids involved in the binding of ligands to TR, RAR, EcR, and LXR.


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